Research workbench
Complete structure of the CORRINOID,IRON-sulfur protein including the N-terminal domain with a 4FE-4S cluster
Analyse Complete structure of the CORRINOID,IRON-sulfur protein including the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YCL
- Type
- protein
- Length
- 751 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carbon monoxide dehydrogenase CORRINOID/IRON-sulfur protein, gamma subunit; Co…
- UniProt
- Q3ACS3, Q3ACS0
- Ligands
- B12, SF4
- Pockets
- 6 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carbon monoxide dehydrogenase CORRINOID/IRON-sulfur protein, gamma subunit | protein | 442 | 45% helix, 17% strand | Q3ACS3 |
| B | Co DEHYDROGENASE/ACETYL-CoA synthase, iron-sulfur protein | protein | 309 | 45% helix, 15% strand | Q3ACS0 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 754 | 0.79 | 0.82 | 78 | B12 |
| 2 | 348 | 0.67 | 0.81 | 33 | empty |
| 3 | 316 | 0.60 | 0.78 | 46 | empty |
| 4 | 100 | 0.38 | 0.75 | 15 | empty |
| 5 | 71 | 0.30 | 0.74 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 2289 Ų buried · 23 hydrogen bonds · protein-protein
Compared structures
- 2YCL · complete structure of the corrinoid,iron-sulfur protein including the N-terminal domain… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q3ACS3
- Every structure of UniProt Q3ACS0
- Elsewhere: RCSB PDB 2YCL · PDBe 2YCL · UniProt Q3ACS3 · UniProt Q3ACS0
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